ID   IMA5_YEAST              Reviewed;         581 AA.
AC   P40884; D6VVY0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Oligo-1,6-glucosidase IMA5;
DE            EC=3.2.1.10;
DE   AltName: Full=Alpha-glucosidase;
DE   AltName: Full=Isomaltase 5;
GN   Name=IMA5; OrderedLocusNames=YJL216C; ORFNames=HRF581, J0228;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7725802; DOI=10.1002/yea.320101216;
RA   Vandenbol M., Durand P., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT   "Sequence analysis of a 40.2 kb DNA fragment located near the left telomere
RT   of yeast chromosome X.";
RL   Yeast 10:1657-1662(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   INDUCTION.
RX   PubMed=12529331; DOI=10.1074/jbc.m208549200;
RA   Hikkel I., Lucau-Danila A., Delaveau T., Marc P., Devaux F., Jacq C.;
RT   "A general strategy to uncover transcription factor properties identifies a
RT   new regulator of drug resistance in yeast.";
RL   J. Biol. Chem. 278:11427-11432(2003).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=20562106; DOI=10.1074/jbc.m110.145946;
RA   Teste M.A., Francois J.M., Parrou J.L.;
RT   "Characterization of a new multigene family encoding isomaltases in the
RT   yeast Saccharomyces cerevisiae, the IMA family.";
RL   J. Biol. Chem. 285:26815-26824(2010).
CC   -!- FUNCTION: Alpha-glucosidase with specificity for isomaltose, maltose,
CC       and palatinose. {ECO:0000269|PubMed:20562106}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some
CC         oligosaccharides produced from starch and glycogen by alpha-amylase,
CC         and in isomaltose.; EC=3.2.1.10;
CC   -!- INDUCTION: Transcriptionally regulated by PDR8. Expression is increased
CC       in response to the addition of maltose, isomaltose, and alpha-
CC       methylglucopyranoside. {ECO:0000269|PubMed:12529331,
CC       ECO:0000269|PubMed:20562106}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; Z34098; CAA83995.1; -; Genomic_DNA.
DR   EMBL; Z49491; CAA89513.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08596.1; -; Genomic_DNA.
DR   PIR; S50769; S50769.
DR   RefSeq; NP_012319.1; NM_001181649.1.
DR   AlphaFoldDB; P40884; -.
DR   SMR; P40884; -.
DR   BioGRID; 33544; 99.
DR   STRING; 4932.YJL216C; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; P40884; -.
DR   PRIDE; P40884; -.
DR   EnsemblFungi; YJL216C_mRNA; YJL216C; YJL216C.
DR   GeneID; 853214; -.
DR   KEGG; sce:YJL216C; -.
DR   SGD; S000003752; IMA5.
DR   VEuPathDB; FungiDB:YJL216C; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   GeneTree; ENSGT00940000176291; -.
DR   HOGENOM; CLU_006462_1_2_1; -.
DR   InParanoid; P40884; -.
DR   OMA; YSTARDV; -.
DR   BioCyc; YEAST:YJL216C-MON; -.
DR   BRENDA; 3.2.1.10; 984.
DR   Reactome; R-SCE-352230; Amino acid transport across the plasma membrane.
DR   PRO; PR:P40884; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P40884; protein.
DR   GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR   GO; GO:0033934; F:glucan 1,4-alpha-maltotriohydrolase activity; IBA:GO_Central.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0004574; F:oligo-1,6-glucosidase activity; IDA:SGD.
DR   GO; GO:0004575; F:sucrose alpha-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0046352; P:disaccharide catabolic process; IGI:SGD.
DR   GO; GO:0000025; P:maltose catabolic process; IBA:GO_Central.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR   GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Maltose metabolism; Reference proteome.
FT   CHAIN           1..581
FT                   /note="Oligo-1,6-glucosidase IMA5"
FT                   /id="PRO_0000054331"
FT   ACT_SITE        210
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   SITE            347
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   581 AA;  67557 MW;  7B65BB7BA583ADF9 CRC64;
     MTIIHNPKWW KEATVYQIYP ASFKDSNNDG WGDLAGITSK LDYVKELGVD AIWVCPFYDS
     PQEDMGYDIA NYEKVWPRYG TNEDCFQMIE EAHKRGIKVI VDLVINHCSE EHEWFKESRS
     SKANPKRDWF FWRPPKGYDE KGNPIPPNNW RSFFGGSAWR YDEKTGEFFL HVFALGQPDF
     NWENEECRKA IYDSSVGYWL RHNVDGFRID VGSMYSKVEG LPDAPITDPT VPYQKGTEFF
     INGPRIHEYH KEMHNYMLSQ VPEGKEIMTV GEVGIGNEDD FRVYTSAKEG ELNMMFNFKH
     TSVGENPKCK YELIPFTLKD FKLALAESFL FIENTDCWST IYLENHDQPR SVSRFGSDSP
     KWREISSKML ATLIISLTGT VFIYQGQELG MPNFKNRKIE QIKCVEGTGT YAAIKRDYGE
     DSEKMKKFFE ALALISRDHG RTPFPWSADE PSAGFSKDAK PWIDMNESFR DGINAEAELK
     DKNSVFFFWK KALQVRKEHK DILVYGHNFQ FIDLDNDKLF MFTKDTDNKK MFAVFNFSSD
     NTDFSVPDNE ASYTMFFGNY ANSNGDSRTL QPWEGRLYLL K